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Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.

Catalytic activityi

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.UniRule annotation
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.UniRule annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Enzyme regulationi

Inhibited by L-buthionine-S-sulfoximine (L-S-BSO).

Kineticsi

  1. KM=22 mM for L-glutamate
  2. KM=156 µM for L-cysteine
  3. KM=8.2 mM for alpha-L-aminobutyrate
  4. KM=64 µM for ATP (in the reaction with gamma-GCS)
  5. KM=5.9 mM for gamma-L-glutamyl-L-cysteine
  6. KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate
  7. KM=6.3 mM for glycine
  8. KM=420 µM for ATP (in the reaction with GS)

    Pathway: glutathione biosynthesis

    This protein is involved in step 1 and 2 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Glutathione biosynthesis bifunctional protein GshAB (gshAB)
    2. Glutathione biosynthesis bifunctional protein GshAB (gshAB)
    This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi696 – 6961Magnesium or manganese 1UniRule annotation
    Metal bindingi717 – 7171Magnesium or manganese 1UniRule annotation
    Metal bindingi717 – 7171Magnesium or manganese 2UniRule annotation
    Metal bindingi719 – 7191Magnesium or manganese 2UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi516 – 57459ATPUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Glutathione biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSAGA208435:GHVY-1917-MONOMER.
    BRENDAi6.3.2.3. 5917.
    SABIO-RKQ8DXM9.
    UniPathwayiUPA00142; UER00209.
    UPA00142; UER00210.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione biosynthesis bifunctional protein GshABUniRule annotation
    Alternative name(s):
    Gamma-GCS-GSUniRule annotation
    Short name:
    GCS-GSUniRule annotation
    Including the following 2 domains:
    Glutamate--cysteine ligaseUniRule annotation (EC:6.3.2.2UniRule annotation)
    Alternative name(s):
    Gamma-ECSUniRule annotation
    Short name:
    GCSUniRule annotation
    Gamma-glutamylcysteine synthetaseUniRule annotation
    Glutathione synthetaseUniRule annotation (EC:6.3.2.3UniRule annotation)
    Alternative name(s):
    GSH synthetaseUniRule annotation
    Short name:
    GSUniRule annotation
    Short name:
    GSH-SUniRule annotation
    Short name:
    GSHaseUniRule annotation
    Glutathione synthaseUniRule annotation
    Gene namesi
    Name:gshABUniRule annotation
    Synonyms:gshFUniRule annotation
    Ordered Locus Names:SAG1821
    OrganismiStreptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
    Taxonomic identifieri208435 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000821 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 750750Glutathione biosynthesis bifunctional protein GshABPRO_0000192559Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.Curated

    Structurei

    Secondary structure

    1
    750
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 93Combined sources
    Beta strandi19 – 3113Combined sources
    Turni32 – 354Combined sources
    Beta strandi44 – 463Combined sources
    Turni49 – 513Combined sources
    Beta strandi53 – 6715Combined sources
    Beta strandi71 – 733Combined sources
    Helixi74 – 9118Combined sources
    Beta strandi96 – 983Combined sources
    Beta strandi101 – 1033Combined sources
    Turni109 – 1113Combined sources
    Helixi120 – 13314Combined sources
    Helixi136 – 1394Combined sources
    Beta strandi143 – 1497Combined sources
    Helixi151 – 16111Combined sources
    Helixi166 – 19126Combined sources
    Beta strandi199 – 2013Combined sources
    Turni206 – 2083Combined sources
    Beta strandi212 – 2143Combined sources
    Beta strandi217 – 2215Combined sources
    Helixi234 – 24310Combined sources
    Turni246 – 2483Combined sources
    Helixi253 – 2553Combined sources
    Beta strandi259 – 2646Combined sources
    Turni268 – 2747Combined sources
    Beta strandi278 – 2814Combined sources
    Helixi296 – 31116Combined sources
    Helixi318 – 33417Combined sources
    Helixi347 – 36115Combined sources
    Helixi365 – 37915Combined sources
    Helixi381 – 3833Combined sources
    Helixi385 – 3928Combined sources
    Helixi399 – 41315Combined sources
    Helixi421 – 4233Combined sources
    Helixi428 – 44013Combined sources
    Beta strandi443 – 4475Combined sources
    Beta strandi449 – 4513Combined sources
    Beta strandi453 – 4586Combined sources
    Beta strandi461 – 4666Combined sources
    Turni467 – 4693Combined sources
    Helixi477 – 4815Combined sources
    Turni482 – 4843Combined sources
    Helixi486 – 4949Combined sources
    Turni507 – 5104Combined sources
    Helixi511 – 5177Combined sources
    Beta strandi518 – 5214Combined sources
    Beta strandi523 – 5275Combined sources
    Beta strandi532 – 5354Combined sources
    Beta strandi537 – 5415Combined sources
    Helixi545 – 55814Combined sources
    Beta strandi560 – 5667Combined sources
    Beta strandi570 – 5789Combined sources
    Beta strandi581 – 5899Combined sources
    Beta strandi592 – 5943Combined sources
    Helixi601 – 6088Combined sources
    Beta strandi614 – 6185Combined sources
    Beta strandi621 – 6233Combined sources
    Helixi629 – 6379Combined sources
    Beta strandi651 – 6544Combined sources
    Turni660 – 6634Combined sources
    Beta strandi665 – 6684Combined sources
    Turni670 – 6723Combined sources
    Helixi675 – 68713Combined sources
    Beta strandi694 – 7007Combined sources
    Beta strandi702 – 7043Combined sources
    Turni708 – 7114Combined sources
    Beta strandi714 – 7218Combined sources
    Helixi725 – 7284Combined sources
    Beta strandi731 – 7333Combined sources
    Helixi739 – 7468Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LN6X-ray2.95A1-750[»]
    ProteinModelPortaliQ8DXM9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini489 – 747259ATP-graspUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 333333Glutamate--cysteine ligaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.UniRule annotation
    Contains 1 ATP-grasp domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1181.
    HOGENOMiHOG000156471.
    KOiK01919.
    OMAiFNPSMYM.
    OrthoDBiEOG6BKJ7H.

    Family and domain databases

    Gene3Di3.30.470.20. 1 hit.
    HAMAPiMF_00782. Glut_biosynth.
    InterProiIPR011761. ATP-grasp.
    IPR013816. ATP_grasp_subdomain_2.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    [Graphical view]
    PfamiPF04262. Glu_cys_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8DXM9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN
    60 70 80 90 100
    YHPYIQTDYS EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP
    110 120 130 140 150
    LSMPPKVREE DIQIAQLEDA FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG
    160 170 180 190 200
    QELLTSLFEL SQADNAIDFQ NQLYMKLSQN FLRYRWLLTY LYGASPVAEE
    210 220 230 240 250
    DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND LENAVKSGQL
    260 270 280 290 300
    IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD
    310 320 330 340 350
    TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL
    360 370 380 390 400
    VDAMQSVIQH FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET
    410 420 430 440 450
    FGQRQGQIYH DYAWEAPYAL KGYETMELST QLLLFDVIQK GVNFEVLDEQ
    460 470 480 490 500
    DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL AMANKVVTKK ILDEKHFPTP
    510 520 530 540 550
    FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK TSANLASYEK
    560 570 580 590 600
    AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT
    610 620 630 640 650
    ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT
    660 670 680 690 700
    KIELRRNSNI STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP
    710 720 730 740 750
    NATQAYSKDK KNATCIELNF NPLMYMHTYC QEGPGQSITP RILAKLFPEL
    Length:750
    Mass (Da):85,603
    Last modified:March 1, 2003 - v1
    Checksum:i97829C2C5B44174A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009948 Genomic DNA. Translation: AAN00684.1.
    RefSeqiNP_688811.1. NC_004116.1.
    WP_000582678.1. NC_004116.1.

    Genome annotation databases

    EnsemblBacteriaiAAN00684; AAN00684; SAG1821.
    GeneIDi1014630.
    KEGGisag:SAG1821.
    PATRICi19630489. VBIStrAga72745_1829.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009948 Genomic DNA. Translation: AAN00684.1.
    RefSeqiNP_688811.1. NC_004116.1.
    WP_000582678.1. NC_004116.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LN6X-ray2.95A1-750[»]
    ProteinModelPortaliQ8DXM9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAN00684; AAN00684; SAG1821.
    GeneIDi1014630.
    KEGGisag:SAG1821.
    PATRICi19630489. VBIStrAga72745_1829.

    Phylogenomic databases

    eggNOGiCOG1181.
    HOGENOMiHOG000156471.
    KOiK01919.
    OMAiFNPSMYM.
    OrthoDBiEOG6BKJ7H.

    Enzyme and pathway databases

    UniPathwayiUPA00142; UER00209.
    UPA00142; UER00210.
    BioCyciSAGA208435:GHVY-1917-MONOMER.
    BRENDAi6.3.2.3. 5917.
    SABIO-RKQ8DXM9.

    Family and domain databases

    Gene3Di3.30.470.20. 1 hit.
    HAMAPiMF_00782. Glut_biosynth.
    InterProiIPR011761. ATP-grasp.
    IPR013816. ATP_grasp_subdomain_2.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    [Graphical view]
    PfamiPF04262. Glu_cys_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-611 / 2603 V/R.
    2. "Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities."
      Janowiak B.E., Griffith O.W.
      J. Biol. Chem. 280:11829-11839(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: ATCC BAA-611 / 2603 V/R.

    Entry informationi

    Entry nameiGSHAB_STRA5
    AccessioniPrimary (citable) accession number: Q8DXM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: March 1, 2003
    Last modified: June 24, 2015
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.